Heme oxygenase: enzyme with functional diversity

Heme oxygenase: enzyme with functional diversity

Автор: Shekhawat G.S., Dixit S., Verma K., Nasybullina E.I., Kosmachevskaya O.V., Topunov A.F.

Журнал: Журнал стресс-физиологии и биохимии @jspb

Статья в выпуске: 1 т.7, 2011 года.

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In recent years role of Heme oxygenase (HO) has been considered in nearly all living system including plants, animals and other organisms. The common role of heme oxygenase is the degradation of heme, although there is a diversity of additional role of HO in organisms including iron acquisition, cellular signaling, defense against stress and biosynthesis during metabolism. Likewise, the function of HO is to provide cofactors for the photosynthetic apparatus in cyanobacteria. Heme concentration is variable in different plant species and found maximum in leguminous plant root nodules. Moreover HO has diverse isoforms in plant and animal systems. The review addressed important function of HO and focused on its functional diversity.

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Heme oxygenase, degradation of heme, antioxidant complex

Короткий адрес: https://sciup.org/14323515

IDR: 14323515

Список литературы Heme oxygenase: enzyme with functional diversity

  • Balestrasse, K.B., Noriega, G.O., Batlle, A. and Tomaro, M.L. (2005) Involvement of heme oxygenase as antioxidant defense in soybean nodules. Free Radical Research, 39, 145-151.
  • Baudouin, E., Frendo, P., Le Gleuher, M. and Puppo, A. (2004) A Medicago sativa hemeoxygenase gene is preferentially expressed in root nodules. J. Exp. Bot., 55, 43-47.
  • Beale, S.I. and Cornejo, J. (1984) Enzymatic heme oxygenase activity in soluble extracts of the unicellular red alga Cyanidium caldarium. Arch. Biochem. Biophys., 235, 371-384.
  • Cornejo, J., Willows, R.D. and Beale, S.I. (1998) Phytobilin biosynthesis: cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC6803. The Plant Journal, 15, 99-107.
  • Davis, S., Bhoo, S.H., Durski, A.M., Walker, J.M. and Viersta, RD. (2001) The heme oxygenase family required for phytochrome chromophore biosynthesis is necessary for proper photomorphogenesis in higher plants. Plant Physiol., 126, 656-669.
  • Elich, T.D., McDonagh, A.F., Palma, L.A. and Lagarias, J.C. (1989) Phytochrome chromophore biosynthesis. Treatment of tetrapyrroledeficient Avena explants with natural and non natural bilatrienes leads to formation of spectrally active holoproteins. J. Biol. Chem., 264, 183-189
  • Emborg, T.J., Walker, J.M., Noh, B. and Vierstra, R.D. (2006) Multiple heme oxygenase family members contribute to the biosynthesis of the phytochrome chromophore in Arabidopsis. Plant Physiol., 140, 856-868.
  • Liu, K., Xu, S., Xuan, W., Ling, T, Cao, Z., Huang, B., Sun, Y., Fang, L., Liu, Z., Zhao, N. and Shen, W. (2007) Carbon monoxide counteracts the inhibition of seed germination and alleviates oxidative damage caused by salt stress in Oryza sativa. Plant Science, 172, 544-555.
  • Maines, M.D. (1997) The heme oxygenase system: A regulator of second messenger genes. Annual Review of Pharmacology and Toxicology, 37, 517-554.
  • Matsumoto, F., Obayashi, T., Sasaki-Sekimoto, Y., Ohta, H., Takamiya, K.-I., and Masuda, T. (2004) Gene expression profiling of the tetrapyrrole metabolic pathway in Arabidopsis with a mini-array system. Plant Physiol., 135, 2379-2391.
  • Muramoto, T., Kohchi, T., Yokota, A., Hwang, I. and Goodman, H.M. (1999) The Arabidopsis photomorphogenic mutant hy1 is deficient in phytochrome chromophore biosynthesis as a result of a mutation in a plastid heme oxygenase. The Plant Cell, 11, 335-348.
  • Reith, M. and Munholland, J. (1995) Complete nucleotide sequence of the Porphyra purpurea chloroplast genome. Plant Mol. Biol. Reports, 13, 333-335.
  • Rhie, G. and Beale, S.I. (1994) Regulation of heme oxygenase activity in Cyanidium caldarium by light, glucose and phycobilin precursors. J. Biol. Chem., 269, 9620-9626.
  • Richaud, C. and Zabulon, G. (1997) The heme oxygenase gene (pbsA) in the red alga Rhodella violacea is discontinuous and transcriptionally activated during iron limitation. Proc. Natl Acad. Sci. USA, 94, 11736-11741.
  • Rudhe, C., Clifton, R., Chew, O., Zemam, K., Richter, S., Lamppa, G., Whelan, J. and Glaser, E. (2004) Processing of the dual targeted precursor protein of glutathione reductase in mitochondria and chloroplasts. J. Mol. Biol., 343, 639-647.
  • Silva-Filho, M.C. (2003) One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Current Opinion in Plant Biology, 6, 589-595.
  • Shekhawat, G.S. and Verma, K. (2010) Heme oxygenase (HO): an overlooked enzyme of plant metabolism and Defense. J. Exp. Botany, 61, 2255-2270.
  • The Arabidopsis Genome Initiative. (2000) Nature, 408, 796-815.
  • Troxler, R.F., Brown, A.S. and Brown, S.B. (1979) Bile pigment synthesis in plants. J. Biol. Chem., 254, 3411-3418.
  • Unno, M., Matsui, T., Ikeda-Saito, M. (2007) Structure and catalytic mechanism of heme oxygenase. Natural Product Reports, 24, 553-570.
  • Vogt, B.A., Alam, J., Croatt, A.J., Vercellotti, G.M. and Nath, K.A. (1995) Acquired resistance to acute renal failure: the role of heme oxygenase and ferritin. Lab. Invest., 72(4), 1-10. 94
  • Yu, C.Z., Benkai, H., Ya, W.Q., Wei, X., Fang, L.T., Bo, Z., Xi, C., Li, N., WenBiao, S. (2007) Involvement of carbon monoxide produced by heme oxygenase in ABA induced stomatal closure in Vicia faba and its proposed signal transduction pathway. Chinese Science Bulletin, 52, 2365-2373.
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